PMID- 15180759
OWN - NLM
STAT- MEDLINE
DCOM- 20050520
LR  - 20121115
IS  - 0105-4538 (Print)
IS  - 0105-4538 (Linking)
VI  - 59
IP  - 7
DP  - 2004 Jul
TI  - Characterization of B- and T-cell responses and HLA-DR4 binding motifs of the 
      latex allergen Hev b 6.01 (prohevein) and its post-transcriptionally formed 
      proteins Hev b 6.02 and Hev b 6.03.
PG  - 724-33
AB  - BACKGROUND: Multiple immunoglobulin E (IgE)-binding proteins in natural rubber 
      latex extracts have been identified. In the case of Hev b 6 a differentiation was 
      made between the precursor protein prohevein (Hev b 6.01) and its two 
      post-transcriptionally formed proteins, the N-terminal hevein (Hev b 6.02) and 
      the C-terminal domain (Hev b 6.03). All three components act as independent 
      allergens. The aim of this study was a detailed analysis of the T-cell responses 
      and the IgE-binding capacity of Hev b 6.01, Hev b 6.02 and Hev b 6.03 by using 
      these allergens as recombinant maltose-binding fusion (MBP) proteins and the 
      usage of synthetic modified hevein peptides. METHODS: Latex-allergic health care 
      workers (HCWs) suffering from rhinitis, conjunctivitis, contact urticaria and/or 
      asthma with increased specific IgE-antibodies to latex were tested for their 
      IgE-binding capacity and T-cell reactivity (by proliferation response) to the 
      recombinant MBP-rHev b 6.01, MBP-rHev b 6.02, MBP-rHev b 6.03, to native Hev b 
      6.02, to modified hevein peptides and wheat germ agglutinin (WGA). For testing of 
      the human leucocyte antigen (HLA) class II restriction of MBP-rHev b 6.01 induced 
      peripheral blood mononuclear cell (PBMC) responses, monoclonal antibodies against 
      HLA-DR, HLA-DP or HLA-DQ were added. RESULTS: Seventeen of 18 (94%) serum samples 
      from latex-allergic HCWs had increased levels of specific IgE to MBP-rHev b 6.01, 
      16 (89%) to MBP-rHev b 6.02 and 13 (72%) to MBP-rHev b 6.03. A significant 
      difference existed between the specific IgE-values of MBP-rHev b 6.02 and 
      MBP-rHev b 6.03 (P < 0.01). Proliferation responses of PBMC of the same 18 
      latex-allergic patients were positive for MBP-rHev b 6.01 and MBP-rHev b 6.03 in 
      83 and 67% of the tested PBMC suspension, whereas the proliferation responses 
      induced with MBP-rHev b 6.02 or native Hev b 6.02 were very low (5.6 and 22.2%). 
      Sera from nine additional latex-allergic patients showed specific IgE binding to 
      the native Hev b 6.02, but none of these sera showed specific IgE binding to the 
      modified Hev b 6.02-peptides [whereby all eight cysteine residues were 
      substituted by serine (C --> S) or by alanine (C --> A)]. Proliferation responses 
      induced by the modified Hev b 6.02 peptides were not significantly different from 
      that induced by Hev b 6.02. Potential HLA-DR4Dw4(DRB1*0401)-restricted T-cell 
      epitopes of Hev b 6.01 predicted by two computer algorithms were only found in 
      the Hev b 6.03-part of Hev b 6.01. CONCLUSION: In the Hev b 6.01 precursor the 
      regions responsible for IgE binding and those for inducing the T-cell 
      proliferation responses are settled in different parts of the protein. The Hev b 
      6.02 domain is responsible for IgE binding and carries discontinuous B-cell 
      epitopes whereas Hev b 6.03 is a better inducer of a proliferation response and 
      contains HLA-DR4-binding motifs.
FAU - Raulf-Heimsoth, M
AU  - Raulf-Heimsoth M
AD  - Research Institute for Occupational Medicine of the Berufsgenossenschaften 
      (BGFA), Institute of the Ruhr-University Bochum, Bochum, Germany.
FAU - Rozynek, P
AU  - Rozynek P
FAU - Bruning, T
AU  - Bruning T
FAU - Rihs, H-P
AU  - Rihs HP
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Denmark
TA  - Allergy
JT  - Allergy
JID - 7804028
RN  - 0 (Allergens)
RN  - 0 (Antigens, Plant)
RN  - 0 (Antimicrobial Cationic Peptides)
RN  - 0 (Epitopes, T-Lymphocyte)
RN  - 0 (HLA-DR4 Antigen)
RN  - 0 (Hev b 6.01 protein, Hevea brasiliensis)
RN  - 0 (Latex)
RN  - 0 (Peptide Fragments)
RN  - 0 (Plant Lectins)
RN  - 0 (Plant Proteins)
RN  - 137295-60-4 (hevein)
RN  - 37341-29-0 (Immunoglobulin E)
SB  - IM
MH  - Adult
MH  - Algorithms
MH  - Allergens/*immunology
MH  - Amino Acid Motifs/immunology
MH  - Amino Acid Sequence
MH  - Antigens, Plant
MH  - Antimicrobial Cationic Peptides/*immunology
MH  - B-Lymphocytes/*immunology
MH  - Epitopes, T-Lymphocyte/immunology
MH  - Female
MH  - HLA-DR4 Antigen/*immunology
MH  - Health Personnel
MH  - Humans
MH  - Immunoglobulin E/blood/immunology
MH  - Latex/*immunology
MH  - Latex Hypersensitivity/blood/immunology
MH  - Male
MH  - Middle Aged
MH  - Molecular Sequence Data
MH  - Peptide Fragments/immunology
MH  - Plant Lectins/*immunology
MH  - Plant Proteins/*immunology
MH  - Predictive Value of Tests
MH  - Protein Processing, Post-Translational
MH  - T-Lymphocytes/*immunology
EDAT- 2004/06/08 05:00
MHDA- 2005/05/21 09:00
CRDT- 2004/06/08 05:00
PHST- 2004/06/08 05:00 [pubmed]
PHST- 2005/05/21 09:00 [medline]
PHST- 2004/06/08 05:00 [entrez]
AID - ALL475 [pii]
AID - 10.1111/j.1398-9995.2004.00475.x [doi]
PST - ppublish
SO  - Allergy. 2004 Jul;59(7):724-33. doi: 10.1111/j.1398-9995.2004.00475.x.